Temperature-dependent solvation modulates the dimensions of disordered proteins

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 14, 2014, Pages 5213-5218

  Wuttke, René ^a   Hofmann, Hagen ^a   Nettels, Daniel ^a   Borgia, Madeleine B ^a   Mittal, Jeetain ^b   Best, Robert B ^c   Schuler, Benjamin ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

^b Lehigh University   (United States)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

ABSINTH; Cold shock protein; HIV integrase; Prothymosin ; Sanchez theory

Indexed keywords

INTRINSICALLY DISORDERED PROTEIN;

ARTICLE; ENERGY TRANSFER; HYDROPHOBICITY; MOLECULE; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; REPRESSOR GENE; SOLVATION; TEMPERATURE DEPENDENCE;

ABSINTH; COLD SHOCK PROTEIN; HIV INTEGRASE; PROTHYMOSIN Α; SANCHEZ THEORY;

FLUORESCENCE RESONANCE ENERGY TRANSFER; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; PROTEIN CONFORMATION; PROTEIN UNFOLDING; SOLUBILITY; TEMPERATURE; THERMODYNAMICS;

EID: 84898039764     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1313006111     Document Type: Article

References (60)

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31. Metcalf WW, van der Donk WA (2009) Biosynthesis of phosphonic and phosphinic acid natural products. Annu Rev Biochem 78(1):65-94.
32. Metcalf WW, et al. (2012) Synthesis of methylphosphonic acid by marine microbes: A source for methane in the aerobic ocean. Science 337(6098):1104-1107.
33. Dyhrman ST, Benitez-Nelson CR, Orchard ED, Haley ST, Pellechia PJ (2009) A microbial source of phosphonates in oligotrophic marine systems. Nat Geosci 2(10):696-699.
34. Dyhrman ST, et al. (2006) Phosphonate utilization by the globally important marine diazotroph Trichodesmium. Nature 439(7072):68-71.
35. Hudson JJ, Taylor WD, Schindler DW (2000) Phosphate concentrations in lakes. Nature 406(6791):54-56.
36. Kamat SS, Raushel FM (2013) The enzymatic conversion of phosphonates to phosphate by bacteria. Curr Opin Chem Biol 17(4):589-596.
37. Pasek MA (2008) Rethinking early Earth phosphorus geochemistry. Proc Natl Acad Sci USA 105(3):853-858.
38. McGrath JW, Chin JP, Quinn JP (2013) Organophosphonates revealed: New insights into the microbial metabolism of ancient molecules. Nat Rev Microbiol 11(6):412-419.
39. Villarreal-Chiu JF, Quinn JP, McGrath JW (2012) The genes and enzymes of phosphonate metabolism by bacteria, and their distribution in the marine environment. Front Microbiol 3(19):19.
40. Jochimsen B, et al. (2011) Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway. Proc Natl Acad Sci USA 108(28):11393-11398.
41. Chen CM, Ye QZ, Zhu ZM, Wanner BL, Walsh CT (1990) Molecular biology of carbonphosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B. J Biol Chem265(8): 4461-4471.
42. Kamat SS, Williams HJ, Raushel FM (2011) Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature 480(7378):570-573.
43. Hove-Jensen B, McSorley FR, Zechel DL (2011) Physiological role of phnP-specified phosphoribosyl cyclic phosphodiesterase in catabolism of organophosphonic acids by the carbon-phosphorus lyase pathway. J Am Chem Soc 133(10):3617-3624.
44. Kamat SS, Williams HJ, Dangott LJ, Chakrabarti M, Raushel FM (2013) The catalytic mechanism for aerobic formation of methane by bacteria. Nature 497(7447):132-136.
45. Frost JW, Loo S, Cordeiro ML, Li D (1987) Radical-based dephosphorylation and organophosphonate biodegradation. J Am Chem Soc 109(7):2166-2171.
46. Martinez A, Tyson GW, Delong EF (2010) Widespread known and novel phosphonate utilization pathways in marine bacteria revealed by functional screening and metagenomic analyses. Environ Microbiol 12(1):222-238.
47. McSorley FR, et al. (2012) PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon-phosphorus bond. J Am Chem Soc 134(20):8364-8367.
48. Aravind L, Koonin EV (1998) The HD domain defines a new superfamily of metaldependent phosphohydrolases. Trends Biochem Sci 23(12):469-472.
49. Solomon EI, et al. (2000) Geometric and electronic structure/function correlations in non-heme iron enzymes. Chem Rev 100(1):235-350.
50. Brown PM, et al. (2006) Crystal structure of a substrate complex of myo-inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolism. Proc Natl Acad Sci USA 103(41):15032-15037.
51. Gosset G, et al. (2008) Investigation of subcellular acidic compartments using α-aminophosphonate 31P nuclear magnetic resonance probes. Anal Biochem 380(2):184-194.
52. Xiang DF, et al. (2009) Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans, a close relative of phosphotriesterase in the amidohydrolase superfamily. Biochemistry 48(10):2237-2247.
53. Holm L, Rosenström P (2010) Dali server: Conservation mapping in 3D. Nucleic Acids Res 38(Web Server issue):W545-9.
54. Bollinger JM, Diao Y, Matthews ML, Xing G, Krebs C (2009) myo-Inositol oxygenase: A radical new pathway for O2 and C-H activation at a nonheme diiron cluster. Dalton Trans (6):905-914.
55. Mashhadi Z, Xu H, White RH (2009) An Fe2+-dependent cyclic phosphodiesterase catalyzes the hydrolysis of 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate in methanopterin biosynthesis. Biochemistry 48(40):9384-9392.
56. van der Donk WA, Krebs C, Bollinger JM, Jr. (2010) Substrate activation by iron superoxo intermediates. Curr Opin Struct Biol 20(6):673-683.
57. Hausinger RP (2004) FeII/α-ketoglutarate-dependent hydroxylases and related enzymes. Crit Rev Biochem Mol Biol 39(1):21-68.
58. Sjögren T, Hajdu J (2001) Structure of the bound dioxygen species in the cytochrome oxidase reaction of cytochrome cd1 nitrite reductase. J Biol Chem 276(16): 13072-13076.
59. Lovering AL, Capeness MJ, Lambert C, Hobley L, Sockett RE (2011) The structure of an unconventional HD-GYP protein from Bdellovibrio reveals the roles of conserved residues in this class of cyclic-di-GMP phosphodiesterases. MBio 2(5):1-8.
60. Wörsdörfer B, et al. (2013) Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases. Proc Natl Acad Sci USA 110(47): 18874-18879.